Carboxylic ester hydrolases in mitochondria from rat skeletal muscle

S Kirkeby; D Moe; T Zelander

Carboxylic ester hydrolases in mitochondria from rat skeletal muscle

S Kirkeby, D Moe, T Zelander

Research output: Contribution to journal › Journal article › Research › peer-review

3 Citations (Scopus)

Abstract

A mitochondrial pellet, prepared from rat skeletal muscle, contained a number of carboxylic ester hydrolase isoenzymes. The esterases which split alpha-naphthyl acetate were organophosphate sensitive, whereas two out of three indoxyl acetate hydrolysing enzymes were resistant to both organophosphate and organomercury. The activity of the indoxyl acetate esterases was enhanced by the non-ionic detergents Tween-40 and Lubrol. After freezing, thawing and high speed centrifugation most of the alpha-naphthyl acetate splitting enzymes were found in the supernatant, indicating that the enzymes are loosely bound to mitochondrial membranes.

Original language	English
Journal	Journal of Molecular Histology (Print Edition)
Volume	22
Issue number	2
Pages (from-to)	95-101
Number of pages	6
ISSN	1567-2379
Publication status	Published - 1990

Bibliographical note

Keywords: Animals; Carboxylic Ester Hydrolases; Centrifugation; Detergents; Edetic Acid; Enzyme Inhibitors; Freezing; Isoenzymes; Male; Mersalyl; Mitochondria, Muscle; Muscles; Rats; Rats, Inbred Strains; Tritolyl Phosphates

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title = "Carboxylic ester hydrolases in mitochondria from rat skeletal muscle",

abstract = "A mitochondrial pellet, prepared from rat skeletal muscle, contained a number of carboxylic ester hydrolase isoenzymes. The esterases which split alpha-naphthyl acetate were organophosphate sensitive, whereas two out of three indoxyl acetate hydrolysing enzymes were resistant to both organophosphate and organomercury. The activity of the indoxyl acetate esterases was enhanced by the non-ionic detergents Tween-40 and Lubrol. After freezing, thawing and high speed centrifugation most of the alpha-naphthyl acetate splitting enzymes were found in the supernatant, indicating that the enzymes are loosely bound to mitochondrial membranes.",

author = "S Kirkeby and D Moe and T Zelander",

note = "Keywords: Animals; Carboxylic Ester Hydrolases; Centrifugation; Detergents; Edetic Acid; Enzyme Inhibitors; Freezing; Isoenzymes; Male; Mersalyl; Mitochondria, Muscle; Muscles; Rats; Rats, Inbred Strains; Tritolyl Phosphates",

year = "1990",

language = "English",

volume = "22",

pages = "95--101",

journal = "Journal of Molecular Histology (Print Edition)",

issn = "1567-2379",

publisher = "Springer",

number = "2",

}

TY - JOUR

T1 - Carboxylic ester hydrolases in mitochondria from rat skeletal muscle

AU - Kirkeby, S

AU - Moe, D

AU - Zelander, T

N1 - Keywords: Animals; Carboxylic Ester Hydrolases; Centrifugation; Detergents; Edetic Acid; Enzyme Inhibitors; Freezing; Isoenzymes; Male; Mersalyl; Mitochondria, Muscle; Muscles; Rats; Rats, Inbred Strains; Tritolyl Phosphates

PY - 1990

Y1 - 1990

N2 - A mitochondrial pellet, prepared from rat skeletal muscle, contained a number of carboxylic ester hydrolase isoenzymes. The esterases which split alpha-naphthyl acetate were organophosphate sensitive, whereas two out of three indoxyl acetate hydrolysing enzymes were resistant to both organophosphate and organomercury. The activity of the indoxyl acetate esterases was enhanced by the non-ionic detergents Tween-40 and Lubrol. After freezing, thawing and high speed centrifugation most of the alpha-naphthyl acetate splitting enzymes were found in the supernatant, indicating that the enzymes are loosely bound to mitochondrial membranes.

AB - A mitochondrial pellet, prepared from rat skeletal muscle, contained a number of carboxylic ester hydrolase isoenzymes. The esterases which split alpha-naphthyl acetate were organophosphate sensitive, whereas two out of three indoxyl acetate hydrolysing enzymes were resistant to both organophosphate and organomercury. The activity of the indoxyl acetate esterases was enhanced by the non-ionic detergents Tween-40 and Lubrol. After freezing, thawing and high speed centrifugation most of the alpha-naphthyl acetate splitting enzymes were found in the supernatant, indicating that the enzymes are loosely bound to mitochondrial membranes.

M3 - Journal article

C2 - 2109744

SN - 1567-2379

VL - 22

SP - 95

EP - 101

JO - Journal of Molecular Histology (Print Edition)

JF - Journal of Molecular Histology (Print Edition)

IS - 2

ER -